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Literature summary for 1.14.14.9 extracted from

  • Wang, L.; Ma, X.; Ruan, H.; Chen, Y.; Gao, L.; Lei, T.; Li, Y.; Gui, L.; Guo, L.; Xia, T.; Wang, Y.
    Optimization of the biosynthesis of B-ring ortho-hydroxylated flavonoids using the 4-hydroxyphenylacetate 3-hydroxylase complex (HpaBC) of Escherichia coli (2021), Molecules, 26, 2919 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis in vivo production of ortho-hydroxylated flavonoids by recombinant Escherichia coli. When HpaC is linked with an S-Tag on the C terminus, the enzyme activity is significantly affected. The optimal culture conditions are a substrate concentration of 80 mg/l, an induction temperature of 28°C, an M9 medium, and a substrate delay time of 6 h after IPTG induction. The efficiency of eriodictyol conversion from recombinant strains fed naringin is up to 57.67. Highest conversion efficiencies for production of catechin and caffeate are 35.2 % and 32.93%, respectively Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli A0A140NG21
-
-
Escherichia coli BL21-DE3 A0A140NG21
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
naringin + NADH + H+ + O2
-
Escherichia coli eryodictyol + NADP+ + H2O
-
?
naringin + NADH + H+ + O2
-
Escherichia coli BL21-DE3 eryodictyol + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
? x * 58500, SDS-PAGE, recombinant protein Escherichia coli